Work will continue on the significance of geometrical packing in the problems of protein structure and folding. Attempts will be made to combine H-bonding requirements and surface area minimization with the present packing algorithms to get a program which will effectively complete partially formed structures. Special attention will be paid to the experimental and theoretical description of the first solvent shell around the folded protein. Work will continue on the development of both general and site specific reagents applicable to studies of the geometry of membrane proteins. Particular attention will be paid to lipid soluble reagents which can label components in the interior of a lipid bilayer. These will be used in conjunction with external probes to monitor the motion of protein components during changes in biological activity.